|
Name |
Accession |
Description |
Interval |
E-value |
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
98-435 |
0e+00 |
|
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273464 [Multi-domain] Cd Length: 455 Bit Score: 644.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 98 ILPDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLA 177
Cdd:TIGR01137 1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 178 LAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDT 257
Cdd:TIGR01137 79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 258 TADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVL 337
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 338 DRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ-ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQK 416
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318
|
330
....*....|....*....
1JBQ_B 417 GFLKEEDLTEKKPWWWHLR 435
Cdd:TIGR01137 319 GFLDDEDLTVKDVLWWHAR 337
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
107-405 |
7.80e-166 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 467.38 E-value: 7.80e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 107 GDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYR 186
Cdd:cd01561 1 GNTPLVRLNRLSP--GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 187 CIIVMPEKMSSEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQC 266
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 267 DGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWF 346
Cdd:cd01561 158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
1JBQ_B 347 KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 405
Cdd:cd01561 233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
97-406 |
2.42e-158 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 448.73 E-value: 2.42e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 97 KILPDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGL 176
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSP--GPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 177 ALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYD 256
Cdd:COG0031 80 AMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 257 TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTV 336
Cdd:COG0031 157 TTGPEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 337 LDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK 406
Cdd:COG0031 232 LDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
96-418 |
3.19e-117 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 345.69 E-value: 3.19e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 96 PKILPDILKKIGDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIG 175
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEATG--CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 176 LALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASN 250
Cdd:PRK10717 79 LALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 251 PLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL----AEPEELNQTEQTTyevE 326
Cdd:PRK10717 158 REAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGELKAEGSSIT---E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 327 GIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK 406
Cdd:PRK10717 235 GIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSK 314
|
330
....*....|..
1JBQ_B 407 FLSDRWMLQKGF 418
Cdd:PRK10717 315 LFNPDFLREKGL 326
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
106-405 |
3.56e-113 |
|
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273465 Cd Length: 298 Bit Score: 333.95 E-value: 3.56e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 106 IGDTPMVRINKIgkkFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGY 185
Cdd:TIGR01139 5 IGNTPLVRLNRI---EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 186 RCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDTTADEILQ 264
Cdd:TIGR01139 82 KLILTMPETMSIERRKLLKAYGAELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 265 QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDK 344
Cdd:TIGR01139 159 DTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRSVIDE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
1JBQ_B 345 WFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 405
Cdd:TIGR01139 234 VITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
102-405 |
2.36e-110 |
|
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273463 Cd Length: 299 Bit Score: 326.93 E-value: 2.36e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 102 ILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAA 181
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAP--GCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 182 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDT 257
Cdd:TIGR01136 79 ARGYKLILTMPETMSLERRKLLRAYGAELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 258 TADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVL 337
Cdd:TIGR01136 152 TGPEIWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKIL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1JBQ_B 338 DRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMT 405
Cdd:TIGR01136 227 DLSLIDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
109-399 |
1.42e-85 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 261.68 E-value: 1.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 109 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLkPGDTIIEPTSGNTGIGLALAAAVRGYRCI 188
Cdd:cd00640 1 TPLVRLKRLSKLGG--ANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 189 IVMPEKMSSEKVDVLRALGAEIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDG 268
Cdd:cd00640 78 IVMPEGASPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 269 -KLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEgsilaepeelnqteqttyevegigydfiptvldrtvvdkWFK 347
Cdd:cd00640 152 qKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE---------------------------------------VVT 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
1JBQ_B 348 SNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDS 399
Cdd:cd00640 193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
106-398 |
4.22e-82 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 254.54 E-value: 4.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 106 IGDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERdgtLKPGDTIIEPTSGNTGIGLALAAAVRGY 185
Cdd:pfam00291 5 IGPTPLVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARLGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 186 RCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQ 265
Cdd:pfam00291 80 KVTIVVPEDAPPGKLLLMRALGAEVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 266 CDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS-ILAEPEELNQTEQTT---YEVEGIGYDFIPTVLDRTV 341
Cdd:pfam00291 154 LGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGALALDL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
1JBQ_B 342 VDKWFKS----NDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA-AQELQEGQRCVVILPD 398
Cdd:pfam00291 234 LDEYVGEvvtvSDEEALEAMRLLARREGIVVEPSSAAALAALKLAlAGELKGGDRVVVVLTG 295
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
102-412 |
3.44e-81 |
|
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a protein of the staphyloferrin B biosynthesis operon of Staphylococcus aureus. SbnA and SbnB together appear to synthesize 2,3-diaminopropionate, a precursor of certain siderophores and other secondary metabolites. SbnA is a pyridoxal phosphate-dependent enzyme. [Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274872 [Multi-domain] Cd Length: 304 Bit Score: 252.51 E-value: 3.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 102 ILKKIGDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAA 181
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAP--FRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 182 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLA 253
Cdd:TIGR03945 79 YKGLRFICVVDPNISPQNLKLLRAYGAEVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 254 HYDTTADEILQQCDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL--AEPeelnqteqTTYEVEGIGYD 331
Cdd:TIGR03945 152 HYHGTGREIARAFP-TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGAS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 332 FIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDR 411
Cdd:TIGR03945 223 VVPELLDESLIDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDE 302
|
.
1JBQ_B 412 W 412
Cdd:TIGR03945 303 W 303
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
100-398 |
6.08e-81 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 251.72 E-value: 6.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 100 PDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALA 179
Cdd:PRK11761 4 PTLEDTIGNTPLVKLQRLPP--DRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 180 AAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDTTA 259
Cdd:PRK11761 82 AAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 260 DEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP-EGS----ILAEPEElnqteqttyevegigydFIP 334
Cdd:PRK11761 158 PEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLP 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
1JBQ_B 335 TVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELqEGQRCVVILPD 398
Cdd:PRK11761 221 KIFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICD 283
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
98-410 |
1.41e-76 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 241.37 E-value: 1.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 98 ILPDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGL 176
Cdd:PLN02565 5 IAKDVTELIGKTPLVYLNNVVD--GCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 177 ALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHY 255
Cdd:PLN02565 83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 256 DTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPT 335
Cdd:PLN02565 159 ETTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1JBQ_B 336 VLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 410
Cdd:PLN02565 234 VLDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
102-405 |
4.49e-72 |
|
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]
Pssm-ID: 130208 [Multi-domain] Cd Length: 290 Bit Score: 228.64 E-value: 4.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 102 ILKKIGDTPMVRINKIGKKFGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAA 181
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGS--EVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 182 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDTTADE 261
Cdd:TIGR01138 80 LKGYRMKLLMPDNMSQERKAAMRAYGAELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 262 ILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEgsilaEPeelnqteqttYEVEGIGY---DFIPTVLD 338
Cdd:TIGR01138 156 IWQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFD 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1JBQ_B 339 RTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQrCVVILPDSVRNYMT 405
Cdd:TIGR01138 221 ASLVDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
101-410 |
1.64e-70 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 225.65 E-value: 1.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 101 DILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPG-DTIIEPTSGNTGIGLALA 179
Cdd:PLN00011 10 DVTELIGNTPMVYLNNIVD--GCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 180 AAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTA 259
Cdd:PLN00011 88 GAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGL---KGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 260 DEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDR 339
Cdd:PLN00011 165 PEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGIIPFNLDL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1JBQ_B 340 TVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQE-GQRCVVILPDSVRNYMTKFLSD 410
Cdd:PLN00011 240 TIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYLSTKLFE 311
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
98-405 |
1.84e-67 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 221.19 E-value: 1.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 98 ILPDILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGL 176
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAK--GCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 177 ALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPL 252
Cdd:PLN03013 191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 253 AHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDF 332
Cdd:PLN03013 264 IHYETTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGF 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1JBQ_B 333 IPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 405
Cdd:PLN03013 339 IPKNLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIY 411
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
81-410 |
5.72e-65 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 212.90 E-value: 5.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 81 PASESPHHHTAPAKSPKILP------DILKKIGDTPMVRINKIGKkfGLKCELLAKCEFFNAGGSVKDRISLRMIEDAER 154
Cdd:PLN02556 26 STVGSPSFAQRLRDLPKDLPgtkiktDASQLIGKTPLVYLNKVTE--GCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 155 DGTLKPGDT-IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRT-PTNARFDSpeshVGVAWRL 232
Cdd:PLN02556 104 KNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTdPTKGMGGT----VKKAYEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 233 KNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPegsilAEP 312
Cdd:PLN02556 180 LESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEP-----AES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 313 EELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQ-EGQR 391
Cdd:PLN02556 255 NVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPEnKGKL 334
|
330
....*....|....*....
1JBQ_B 392 CVVILPDSVRNYMTKFLSD 410
Cdd:PLN02556 335 IVTVHPSFGERYLSSVLFQ 353
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
102-418 |
1.13e-56 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 192.51 E-value: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 102 ILKKIGDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAA 181
Cdd:PLN02356 47 LIDAIGNTPLIRINSLSEATG--CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 182 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRT-PTNarFDSPESHVGVAWRL---KNEIPNSHIL--------------- 242
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVrPVS--ITHKDHYVNIARRRaleANELASKRRKgsetdgihlektngc 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 243 ---------------------DQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIG 301
Cdd:PLN02356 203 iseeekenslfsssctggffaDQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 302 VDPEGSIL--------------AEPEELNQTEQTTyeVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 367
Cdd:PLN02356 283 IDPPGSGLfnkvtrgvmytreeAEGRRLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLF 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
1JBQ_B 368 CGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGF 418
Cdd:PLN02356 361 VGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGL 411
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
109-396 |
5.99e-30 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 117.97 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 109 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRISLRMI----EDAERDGtlkpgdtIIEPTSGNTGIGLALAAAVRG 184
Cdd:cd01562 18 TPLLTSPTLSELLG--AEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 185 YRCIIVMPEKMSSEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD--- 256
Cdd:cd01562 89 IPATIVMPETAPAAKVDATRAYGAEVVL--YGEDFDEAEAK---ARELAEEegltfIH-------------PFDDPDvia 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 257 ---TTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTEQTtyeVE 326
Cdd:cd01562 151 gqgTIGLEILEQV-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTI---AD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1JBQ_B 327 GIGydfIPTVLDRT------VVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 396
Cdd:cd01562 227 GLA---VKRPGELTfeiirkLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALA-ALLSGKLDLKGKKVVVVL 298
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
109-396 |
8.16e-30 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 117.83 E-value: 8.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 109 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDR------ISLRmieDAERDGTlkpgdtIIEPTSGNTGIGLALAAAV 182
Cdd:COG1171 25 TPLLRSPTLSERLG--AEVYLKLENLQPTGSFKLRgaynalASLS---EEERARG------VVAASAGNHAQGVAYAARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 183 RGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD- 256
Cdd:COG1171 94 LGIPATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAA---AAELAEEegatfVH-------------PFDDPDv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 257 -----TTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTeQT--- 321
Cdd:COG1171 156 iagqgTIALEILEQL-PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTiad 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1JBQ_B 322 ---TYEVEGIGYDFIPTVLDRTV-VDkwfksnDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 396
Cdd:COG1171 234 glaVGRPGELTFEILRDLVDDIVtVS------EDEIAAAMRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVVL 305
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
109-396 |
3.61e-28 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 113.25 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 109 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGY 185
Cdd:PRK06815 21 TPLEHSPLLSQHTG--CEVYLKCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 186 RCIIVMPEKMSSEKVDVLRALGAEIVRTPTNArfDSPESHvgvAWRLKNEIPNSHIlDQYrNASNPLAHYDTTADEILQQ 265
Cdd:PRK06815 93 PVTVYAPEQASAIKLDAIRALGAEVRLYGGDA--LNAELA---ARRAAEQQGKVYI-SPY-NDPQVIAGQGTIGMELVEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 266 CDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA----EPEELNQTEQTTyeVEGIGYDFIPT 335
Cdd:PRK06815 166 QP-DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTLSDGT--AGGVEPGAITF 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
1JBQ_B 336 VLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQeGQRCVVIL 396
Cdd:PRK06815 243 PLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQ-GKKVAVVL 302
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
99-396 |
1.39e-20 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 91.89 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 99 LPDILKKI-----GDTPMVRINKIGKKFGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTG 173
Cdd:cd01563 8 LPVTEDDIvslgeGNTPLVRAPRLGERLGGK-NLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 174 IGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLA 253
Cdd:cd01563 83 ASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 254 H--YDTTADEILQQCDGKL-DMLVASVGTGGTITGIARKLKE--------KCPgcRIIGVDPEGS------ILAEPEELN 316
Cdd:cd01563 153 LegQKTIAFEIAEQLGWEVpDYVVVPVGNGGNITAIWKGFKElkelglidRLP--RMVGVQAEGAapivraFKEGKDDIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 317 QTEQTTYEVEGIGydfIPT-VLDRTVVDKWFKSN------DEEAFTFARMLIAQ-EGLLCGGSAGSTVAVAVKAAQE--L 386
Cdd:cd01563 231 PVENPETIATAIR---IGNpASGPKALRAVRESGgtavavSDEEILEAQKLLARtEGIFVEPASAASLAGLKKLREEgiI 307
|
330
....*....|
1JBQ_B 387 QEGQRCVVIL 396
Cdd:cd01563 308 DKGERVVVVL 317
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
104-396 |
2.23e-19 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 88.22 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 104 KKIGDTPMVRINKIGKKFGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVR 183
Cdd:PRK06381 11 KPPGGTPLLRARKLEEELGLR-KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 184 GYRCIIVMPEKMSSEKVDVLRALGAEIVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDTTAD 260
Cdd:PRK06381 86 GLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 261 EILQQCDGKLDMLVASVGTGGTITGIARKLKE--------KCPgcRIIGVDPEGS--------------ILAEPEELNQT 318
Cdd:PRK06381 158 EIYEALGDVPDAVAVPVGNGTTLAGIYHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 319 EQTTYEVEGIGYDFiPTVLD--RTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVIL 396
Cdd:PRK06381 236 AVNEPLVSYRSFDG-DNALEaiYDSHGYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
107-403 |
1.27e-16 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 81.01 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 107 GDTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDR-----ISLrmiedAERDGTlkpgDTIIEPTSGNTGIGLALAAA 181
Cdd:COG0498 65 GGTPLVKAPRLADELG--KNLYVKEEGHNPTGSFKDRamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 182 VRGYRCIIVMPE-KMSSEKVDVLRALGAEIVRTPTNarFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPLAH--YDT 257
Cdd:COG0498 134 RAGIEVFVFVPEgKVSPGQLAQMLTYGAHVIAVDGN--FD-------DAQRLVKELAADEGL--YaVNSINPARLegQKT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 258 TADEILQQCDGKLDMLVASVGTGGTITGI--ARK------LKEKCPgcRIIGVDPEGS--ILAEPEelnqTEQTTYEVEG 327
Cdd:COG0498 203 YAFEIAEQLGRVPDWVVVPTGNGGNILAGykAFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDEYEPER 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 328 ---------IGydfIPT-------VLDRTvvDKWF-KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQE 388
Cdd:COG0498 277 petiapsmdIG---NPSngeralfALRES--GGTAvAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDP 351
|
330 340
....*....|....*....|..
1JBQ_B 389 GQRCVVIL-------PDSVRNY 403
Cdd:COG0498 352 DEPVVVLStghglkfPDAVREA 373
|
|
| PLN02970 |
PLN02970 |
serine racemase |
126-307 |
3.93e-16 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 78.95 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 126 ELLAKCEFFNAGGSVKDRISLRMI-----EDAERDgtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKV 200
Cdd:PLN02970 43 SLFFKCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 201 DVLRALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDTTADEILQQCDGkLDMLVASVGT 279
Cdd:PLN02970 115 DAVIRYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEFLEQVPE-LDVIIVPISG 185
|
170 180
....*....|....*....|....*...
1JBQ_B 280 GGTITGIARKLKEKCPGCRIIGVDPEGS 307
Cdd:PLN02970 186 GGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
170-307 |
2.56e-14 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 74.79 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 170 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 244
Cdd:PRK09224 77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1JBQ_B 245 yrnasnPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 307
Cdd:PRK09224 145 ------PFDDPDviagqgTIAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
126-307 |
2.75e-14 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 73.07 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 126 ELLAKCEFFNAGGSVKDRISLRMIEDAErdgtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRA 205
Cdd:PRK08246 38 PVWLKLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 206 LGAEIVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDTTADEILQQCdGKLDMLVASVGTG 280
Cdd:PRK08246 113 LGAEVVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIEEQA-PGVDTVLVAVGGG 179
|
170 180
....*....|....*....|....*..
1JBQ_B 281 GTITGIARKLKekcPGCRIIGVDPEGS 307
Cdd:PRK08246 180 GLIAGIAAWFE---GRARVVAVEPEGA 203
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
126-305 |
2.90e-14 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 73.13 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 126 ELLAKCEFFNAGGSVKDR---ISLRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV 202
Cdd:PRK07048 40 QVFFKCENFQRMGAFKFRgayNALSQFSPEQR----RAG--VVTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 203 LRALGAEIVRtptnarFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKL 270
Cdd:PRK07048 114 TRGYGGEVVT------YDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELFEEV-GPL 173
|
170 180 190
....*....|....*....|....*....|....*
1JBQ_B 271 DMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 305
Cdd:PRK07048 174 DALFVCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
164-307 |
3.47e-13 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 71.37 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 164 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEIPNS--HI 241
Cdd:PRK12483 88 VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAH---ALKLAEEEGLTfvPP 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1JBQ_B 242 LDQyrnaSNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 307
Cdd:PRK12483 163 FDD----PDVIAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
102-304 |
1.00e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 65.95 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 102 ILKKIGDTPMVRINKIGKKFGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERDGtlKPGDTIIEPTSGNTGIGLALAAA 181
Cdd:PRK06608 17 IKQYLHLTPIVHSESLNEMLGH--EIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 182 VRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDTT 258
Cdd:PRK06608 93 LFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
1JBQ_B 259 ADEILQQCDGKLDMLVASVGTGGTITG--IARKLKEkcPGCRIIGVDP 304
Cdd:PRK06608 161 CYEALQQLGFSPDAIFASCGGGGLISGtyLAKELIS--PTSLLIGSEP 206
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
97-293 |
1.77e-11 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 65.10 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 97 KILPDILKKI-----GDTPMVRINKIGKKFGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGN 171
Cdd:TIGR00260 6 EFLPVTEKDLvdlgeGVTPLFRAPALAANVGIK-NLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 172 TGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVLRALGAEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnSHIL 242
Cdd:TIGR00260 81 TGAAAAAYAGKAGLKVVVLYPAgKISLGKLAQALGYNAEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-YRLE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1JBQ_B 243 DQYrnasnplahydTTADEILQQCDGKL-DMLVASVGTGGTITGIARKLKEK 293
Cdd:TIGR00260 158 GQK-----------TYAFEAVEQLGWEApDKVVVPVPNSGNFGAIWKGFKEK 198
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
102-305 |
6.53e-11 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 63.22 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 102 ILKKIGDTPMVRINKIGKKfgLKCELLAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLAL 178
Cdd:PRK08638 21 LAGRIRKTPLPRSNYLSER--CKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEK----RKG--VVACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 179 AAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILDQYrNASNPLAHYDTT 258
Cdd:PRK08638 93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIPPY-DDPKVIAGQGTI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
1JBQ_B 259 ADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 305
Cdd:PRK08638 166 GLEILEDL-WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSE 211
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
109-307 |
2.42e-09 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 58.46 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 109 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDR-ISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRC 187
Cdd:cd06448 2 TPLIESTALSKTAG--CNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 188 IIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDTTADEILQQ 265
Cdd:cd06448 78 TIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
1JBQ_B 266 C--DGKLDMLVASVGTGGTITGIARKLkEKCPGCR--IIGVDPEGS 307
Cdd:cd06448 151 LqsQEKVDAIVCSVGGGGLLNGIVQGL-ERNGWGDipVVAVETEGA 195
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
108-304 |
1.12e-08 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 57.24 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 108 DTPMVRINKIGKKFGLKceLLAKCEFFNAGGSVKDRISLRMIEDAERDgTLKPGdtIIEPTSGNTGIGLALAAAVRGYRC 187
Cdd:PLN02550 109 ESPLQLAKKLSERLGVK--VLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 188 IIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVgvawrlkneipNSHILDQYRNASNPLAHYD------TTADE 261
Cdd:PLN02550 184 VIAMPVTTPEIKWQSVERLGATVVLVGDS--YDEAQAYA-----------KQRALEEGRTFIPPFDHPDviagqgTVGME 250
|
170 180 190 200
....*....|....*....|....*....|....*....|...
1JBQ_B 262 ILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP 304
Cdd:PLN02550 251 IVRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEP 293
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
257-306 |
1.23e-08 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 56.74 E-value: 1.23e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
1JBQ_B 257 TTADEILQQCD--GKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG 306
Cdd:PRK08639 165 TVAVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
109-305 |
2.09e-08 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 56.04 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 109 TPMVRINKIGKKFGLKcELLAKCE---F----FNA-GGS------VKDRISLRMIE---DAERDGTLKP--GD-TIIEPT 168
Cdd:PRK08206 45 TPLVALPDLAAELGVG-SILVKDEsyrFglnaFKAlGGAyavarlLAEKLGLDISElsfEELTSGEVREklGDiTFATAT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 169 SGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDspEShVGVAWRLKNEipNSHILDQyrNA 248
Cdd:PRK08206 124 DGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN--YD--DS-VRLAAQEAQE--NGWVVVQ--DT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1JBQ_B 249 SNP---------LAHYDTTADEILQQCDGKLD-----MLVASVGT--GGTITGIARKLKEKCPgcRIIGVDPE 305
Cdd:PRK08206 195 AWEgyeeiptwiMQGYGTMADEAVEQLKEMGVppthvFLQAGVGSlaGAVLGYFAEVYGEQRP--HFVVVEPD 265
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
97-305 |
3.50e-08 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 54.74 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 97 KILPDILKKI----GDTPMVRINKIgkKFglkcellaKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNT 172
Cdd:PRK06450 43 KNFPYIKHFIslgeGRTPLIKKGNI--WF--------KLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 173 GIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYRN 247
Cdd:PRK06450 109 GASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAEVVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFRD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1JBQ_B 248 ASNPLAHydttadEILQQCDGKL-DMLVASVGTGGTITGIARKLK--------EKCPgcRIIGVDPE 305
Cdd:PRK06450 179 GIRTLAY------EIAKDLDWKIpNYVFIPVSAGTLLLGVYSGFKhlldsgviSEMP--KIVAVQTE 237
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
123-211 |
7.48e-08 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 53.84 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 123 LKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV 202
Cdd:PRK06110 34 LGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAA 111
|
....*....
1JBQ_B 203 LRALGAEIV 211
Cdd:PRK06110 112 MRALGAELI 120
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
108-305 |
1.14e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 53.74 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 108 DTPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRG 184
Cdd:PRK07334 23 RTPCVHSRTLSQITG--AEVWLKFENLQFTASFKERGAlnkLLLLTEEER----ARG--VIAMSAGNHAQGVAYHAQRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 185 YRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEipnshildQYRNASNPLAHYD------TT 258
Cdd:PRK07334 95 IPATIVMPRFTPTVKVERTRGFGAEVVLH--GETLDEARAH---ARELAEE--------EGLTFVHPYDDPAviagqgTV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
1JBQ_B 259 ADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 305
Cdd:PRK07334 162 ALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTE 207
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
97-399 |
7.03e-07 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 51.35 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 97 KILPDILKKI----GDTPMVRiNKIGKKFGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNT 172
Cdd:PRK05638 51 ELLPQVKKIIslgeGGTPLIR-ARISEKLGE--NVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 173 GIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnas 249
Cdd:PRK05638 124 AASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 250 npLAHYDTTADEILQQCDGklDMLVASVGTGGTITGIARKLKE--------KCPgcRIIGVDPE------GSILAEPEEL 315
Cdd:PRK05638 196 --LEGQKTIAFELWEEINP--THVIVPTGSGSYLYSIYKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKC 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 316 NQTeqttyevEGIGYDFIPTVLDRTVVDKWFKS------NDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQ 387
Cdd:PRK05638 270 NET-------KALGLYVKNPVMKEYVSEAIKESggtavvVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIE 342
|
330
....*....|..
1JBQ_B 388 EGQRCVVILPDS 399
Cdd:PRK05638 343 KGDKVVLVVTGS 354
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
63-212 |
1.58e-06 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 50.00 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 63 PLWIRPD-APSRCTWQ----LGRPASESPHHHTAPAKSPKILPDILKkiGDTPMVRINKIGKKFGLKcELLAKCEFFNAG 137
Cdd:PRK08197 31 PLLVRYDlEAVKQAVTrealAGRPANLWRYHELLPVRDPEHIVSLGE--GMTPLLPLPRLGKALGIG-RLWVKDEGLNPT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1JBQ_B 138 GSVKDRISLRMIEDAERDGTLKpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVR 212
Cdd:PRK08197 108 GSFKARGLAVGVSRAKELGVKH----LAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAGAELYL 178
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
96-306 |
3.15e-06 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 49.05 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 96 PKILPDIlkkigdTPMVRINKigkkfglkcELLAKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIG 175
Cdd:PRK08329 58 PHLTPPI------TPTVKRSI---------KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 176 LALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIvrtpTNARFDSPESHV-GVAWRLKNEIPN-SHILDQYRnasnpLA 253
Cdd:PRK08329 119 LALYSLSEGIKVHVFVSYNASKEKISLLSRLGAEL----HFVEGDRMEVHEeAVKFSKRNNIPYvSHWLNPYF-----LE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1JBQ_B 254 HYDTTADEILQQCdGKLDMLVASVGTGGTITGIARKLKE--------KCPgcRIIGVDPEG 306
Cdd:PRK08329 190 GTKTIAYEIYEQI-GVPDYAFVPVGSGTLFLGIWKGFKElhemgeisKMP--KLVAVQAEG 247
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
109-302 |
4.33e-06 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 48.42 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 109 TPMVRINKIGKKFGlkCELLAKCEFFNAGGSVKDR----ISLRMIEDAERDGtlkpgdtIIEPTSGNTGIGLALAAAVRG 184
Cdd:PRK07476 20 TPLVASASLSARAG--VPVWLKLETLQPTGSFKLRgatnALLSLSAQERARG-------VVTASTGNHGRALAYAARALG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 185 YRCIIVMPEKMSSEKVDVLRALGAEIVRTPtnarfDSPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD--- 256
Cdd:PRK07476 91 IRATICMSRLVPANKVDAIRALGAEVRIVG-----RSQDDAQAEVERLVREegltmVP-------------PFDDPRiia 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
1JBQ_B 257 ---TTADEILQQCDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGV 302
Cdd:PRK07476 153 gqgTIGLEILEALP-DVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGV 200
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
109-367 |
8.63e-06 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 47.42 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 109 TPMVRINKIGKKFGLKCELLAKCEFFN---AGGSVKDRISLRMIEDAERDGTlkpgDTIIepTSG----NTGIGLALAAA 181
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVEIYAKRDDCNsglAFGGNKIRKLEYLLPDALAKGA----DTLV--TVGgiqsNHTRQVAAVAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 182 VRGYRCIIVM--PEKMSSEKVD------VLRALGAEIvrtptnaRFDSPESHVGV-------AWRLKNE------IPNSh 240
Cdd:cd06449 75 KLGLKCVLVQenWVPYSDAVYDrvgnilLSRIMGADV-------RLVSAGFDIGIrksfeeaAEEVEAKggkpyvIPAG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 241 ildqyrNASNPLAH--YDTTADEILQQCDG---KLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEEL 315
Cdd:cd06449 147 ------GSEHPLGGlgYVGFVLEIAQQEEElgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQV 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
1JBQ_B 316 NQTEQTTYEVEGIGYdfipTVLDRTVVDKWF-----KSNDE--EAFtfaRMLIAQEGLL 367
Cdd:cd06449 221 LRIAQAKLAEEGLEV----KEEDVVLDDDYAapeygIPNDEtiEAI---KLCARLEGII 272
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
151-302 |
2.13e-05 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 46.36 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 151 DAERDGTlkpgDTIIepTSGntGIG-----LALAAAVR-GYRCIIVMPEKMSSEKVDVL--------RALGAEIVRTPTN 216
Cdd:PRK03910 58 DALAQGA----DTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 217 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDTTADEILQQCDG---KLDMLVASVGTGGTITG 285
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
|
170
....*....|....*..
1JBQ_B 286 IARKLKEKCPGCRIIGV 302
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV 216
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
147-213 |
4.65e-05 |
|
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176250 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 4.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 147 RMIEDAerdGTLKPGDTIIEpTSGNTGIGLALA--AAVRGYRCIIVMPEKMSSEK-VDVLRALGAEIVRT 213
Cdd:cd08290 136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
107-301 |
5.58e-04 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 42.11 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 107 GDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTL-KPGDTIIEPTSGNTGIGLALAAAVRGY 185
Cdd:PLN02569 132 GNSNLFWAERLGKEFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYCAAAGI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JBQ_B 186 RCIIVMPE-KMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIP----NShiLDQYRnasnpLAHYDTTAD 260
Cdd:PLN02569 212 PSIVFLPAdKISIAQLVQPIANGALVLSIDTD--FDGCMRLIR---EVTAELPiylaNS--LNSLR-----LEGQKTAAI 279
|
170 180 190 200
....*....|....*....|....*....|....*....|..
1JBQ_B 261 EILQQCDGKL-DMLVASVGTGGTITGIARKLKEkcpgCRIIG 301
Cdd:PLN02569 280 EILQQFDWEVpDWVIVPGGNLGNIYAFYKGFKM----CKELG 317
|
|
| |
